We propose to perform time-resolved SAXS measurements of the small all beta sheet alpha amylase protein, tendamistat. It is known from optical kinetic measurements that this protein folds directly to the native state in around 5 millisecs without going through a partially folded intermediate. We plan to measure changes of the radius of gyration of the protein unfolding under conditions where the rate constant for folding may be slowed down to a rate between 50 millisecs to 1 sec by increasing the final denaturant concentration and/or by using a mutant protein with a decreased folding rate. This will enable us to test the hypothesis that a non-specific polymer collapse must occur before the transition state to the native conformation is entered.